transferase

Transferase is a class of enzymes that catalyze the transfer of a functional group from one molecule (the donor) to another (the acceptor). This core activity enables the modification, synthesis, and interconversion of a wide range of biomolecules, making transferases central to metabolism, biosynthesis, and regulation. In enzyme nomenclature, transferases are grouped in EC class 2, which is characterized by group transfer reactions.

Subtypes of transferases transfer many different groups, including phosphate, glycosyl, acyl, amino, and methyl groups. Examples include kinases (phosphotransferases) that move phosphate groups from ATP to substrates; aminotransferases that transfer amino groups between amino acids and α-keto acids; methyltransferases that relocate methyl groups; glycosyltransferases that attach sugar moieties to proteins or lipids; and acetyltransferases or other acyltransferases that transfer acyl groups. These enzymes participate in fundamental processes such as energy metabolism, nucleotide and carbohydrate synthesis, protein modification, and DNA or RNA processing.

Mechanistically, transferases often rely on an activated donor molecule and may require cofactors or metal ions. The donor’s activated group is transferred to an appropriate acceptor, with reaction energetics and specificity governed by the enzyme’s active site and structural features. Transferases operate in various cellular compartments and pathways, reflecting their diverse biological roles.

Clinical and biotechnological relevance is broad. Defects or altered activity of transferases can contribute to metabolic disorders or disease states, while transferases serve as targets in drug development and as tools in the synthesis of pharmaceuticals, biopolymers, and other bioactive compounds.